Publikationsdatum:
1982-11-05
Beschreibung:
Receptors for maleylated or acetylated proteins as well as for alpha-2-macroglobulin-protease complexes on macrophages serve as scavengers by mediating the uptake of macromolecules from the extracellular compartment. Described in this report is a novel function of these receptors on macrophages: regulation of neutral protease secretion. The binding of maleylated bovine serum albumin to macrophages triggered secretion of three neutral proteases: neutral caseinases, plasminogen activator, and cytolytic proteinase. Release of acid phosphatase, however, was not induced. An important biological consequence of protease secretion by macrophages, tumor-cytolysis, was also triggered by engagement of the receptor for maleylated bovine serum albumin. By contrast, the binding of alpha-2-macroglobulin-protease complexes to the macrophages suppressed secretion of all three proteases. Thus two receptors heretofore believed to serve principally as scavengers also regulate secretory functions of macrophages.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, W J -- Pizzo, S V -- Imber, M J -- Adams, D O -- New York, N.Y. -- Science. 1982 Nov 5;218(4572):574-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6289443" target="_blank"〉PubMed〈/a〉
Schlagwort(e):
Animals
;
Cells, Cultured
;
Glycoproteins/*metabolism
;
Macrophages/*enzymology
;
*Metalloendopeptidases
;
Mice
;
Peptide Hydrolases/*secretion
;
Plasminogen Activators/secretion
;
Receptors, Cell Surface/*physiology
Print ISSN:
0036-8075
Digitale ISSN:
1095-9203
Thema:
Biologie
,
Chemie und Pharmazie
,
Informatik
,
Medizin
,
Allgemeine Naturwissenschaft
,
Physik
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